The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

The site of ubiquinone binding observed in the cryo-EM structure of respiratory complex I during turnover supports a two-state stabilization change mechanism.

The cyclic-peptide antibiotic GE23077 inhibits bacterial RNA polymerase through a novel target that exhibits low susceptibility to target-based resistance and that enables synthesis of bipartite inhibitors that are exceptionally potent and refractory to target-based resistance.

Chemical modifications near the tRNA anticodon and specific mRNA–tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.

Structure of the portal protein of a thermostable virus, determined in its capsid-bound state, reveals a molecular mechanism that prevents DNA slippage during genome packaging.

Minimal changes allow an ancestral, unfolded peptide to adopt a known fold by repetition, illuminating a possible path for the emergence of folded proteins at the origin of life.

The crystal structure of Thermus transcription activation complexes containing the transcriptional activator CarD reveals a new mechanism for the activation of transcription.